Turnover of receptor tyrosine kinases regulated by membrane trafficking
| Project/Area Number |
26830080
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Tumor biology
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| Research Institution | Fukushima Medical University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
WAGURI SATOSHI 福島県立医科大学, 医学部, 教授 (30244908)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2016: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2015: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2014: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Keywords | ゴルジ体 / エンドソーム / 受容体型チロシンキナーゼ / 小胞輸送 / タンパク寿命調節 / ノックダウン / 細胞増殖 / 癌 / 上皮成長因子受容体 / 細胞膜 / クラスリンアダプター / 細胞膜受容体 / 細胞内小胞輸送 |
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| Outline of Final Research Achievements |
GGAs (GGA1,2,3) and AP-1 are membrane trafficking associated molecules and they function as clathrin adaptors. Their functions have been investigated in terms of quality control of protein using cell lines. Depletion of GGA2 or AP-1 complex decreased EGFR expression at protein level, reflecting enhanced lysosomal degradation of EGFR. This result suggests that GGA2 and AP-1 complex are involved in protein transport of transmembrane protein at the post-Golgi compartments to regulate the turnover. Also, this raises a possibility that the malfunction of GGAs and AP-1 could influence pathologies such as neurodegenerative diseases or cancer.
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Report
(4 results)
Research Products
(15 results)
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[Journal Article] p62/Sqstm1 promotes malignancy of HCV-positive hepatocellular carcinoma through Nrf2-dependent metabolic reprogramming2016
Author(s)
Saito T, Ichimura Y, Taguchi K, Suzuki T, Mizushima T, Takagi K, Hirose Y, Nagahashi M, Iso T, Fukutomi T, Ohishi M, Endo K, Uemura T, Nishito Y, Okuda S, Obata M, Kouno T, Imamura R, Tada Y, Obata R, Yasuda D, Takahashi K, Fujimura T, Pi J, Lee MS, Ueno T, Ohe T, Mashino T, Wakai T, Kojima H, Okabe T, Nagano T et al.
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Journal Title
Nature Commun
Volume: 7
Issue: 1
Pages: 12030-12030
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Journal Article] Differing susceptibility to autophagic degradation activity of two LC3-binding proteins: SQSTM1/p62 and TBC1D25/OATL1.2016
Author(s)
Hirano, S., Uemura, T., Annoh, H., Fujita, N., Waguri, S., Itoh, T. and Fukuda, M.
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Journal Title
Autophagy
Volume: 12
Issue: 2
Pages: 312-326
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research / Acknowledgement Compliant
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[Journal Article] Proteasome dysfunction activates autophagy and the Keap1-Nrf2 pathway2014
Author(s)
Kageyama S, Sou YS, Uemura T, Kametaka S, Saito T, Ishimura R, Kouno T, Bedford L, Mayer RJ, Lee MS, Yamamoto M, Waguri S, Tanaka K, and Komatsu M.
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Journal Title
J Biol Chem
Volume: 289
Issue: 36
Pages: 24944-24955
DOI
Related Report
Peer Reviewed / Open Access
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